Characterization of laminin isoforms in human amnion

Seiji Takashima, Masanori Yasuo, Noriko Sanzen, Kiyotoshi Sekiguchi, Motonori Okabe, Toshiko Yoshida, Ayaka Toda, Toshio Nikaido*

*この論文の責任著者

研究成果: ジャーナルへの寄稿学術論文査読

30 被引用数 (Scopus)

抄録

Epithelial cells of the human amnion have been reported to possess similar functions to many types of cells, such as hepatocytes, neurons, and pancreatic β-cells. We reported previously that one of the hepatocyte-like functions of human amniotic epithelial cells was reinforced by the presence of basement membrane components. Laminin is one of the main components of the basement membrane; it critically contributes to cell differentiation. Laminin has several heterotrimer isoforms composed of an α-, a β-, and a γ-chain, and each type of chain has several types of subunit chains: α1-5, β1-3, and γ1-3. In this study, we characterized the laminin subunit chains in human amnion. Laminin is produced and secreted from adjacent epithelial cells, and therefore, the gene expression of laminin subunit chains in human amniotic epithelial cells was investigated by RT-PCR. Their localization was examined by immunohistochemical staining of frozen sections. The findings suggested that the basement membrane of the human amnion contains a broad spectrum of laminin isoforms, laminin-2, -4, -5, -6, -7, -10, -11. These findings will provide clues not only for understanding the physiological roles of the amnion and hAECs, but also for applying this tissue as a source of donor cells for cell transplantation therapy.

本文言語英語
ページ(範囲)75-81
ページ数7
ジャーナルTissue and Cell
40
2
DOI
出版ステータス出版済み - 2008/04

ASJC Scopus 主題領域

  • 発生生物学
  • 細胞生物学

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